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Fibroblast growth factor 5 (FGF-5) (Heparin-binding growth factor 5) (HBGF-5) (Smag-82)

 FGF5_HUMAN              Reviewed;         268 AA.
P12034; B2R554; O75846; Q3Y8M3; Q8NF90;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
24-JAN-2006, sequence version 4.
25-OCT-2017, entry version 164.
RecName: Full=Fibroblast growth factor 5;
Short=FGF-5;
AltName: Full=Heparin-binding growth factor 5;
Short=HBGF-5;
AltName: Full=Smag-82;
Flags: Precursor;
Name=FGF5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
TISSUE=Brain stem;
PubMed=1700424; DOI=10.1073/pnas.87.20.8022;
Haub O., Drucker B., Goldfarb M.;
"Expression of the murine fibroblast growth factor 5 gene in the adult
central nervous system.";
Proc. Natl. Acad. Sci. U.S.A. 87:8022-8026(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3211147; DOI=10.1128/MCB.8.8.3487;
Zhan X., Bates B., Hu X., Goldfarb M.;
"The human FGF-5 oncogene encodes a novel protein related to
fibroblast growth factors.";
Mol. Cell. Biol. 8:3487-3495(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
Ozawa K., Suzuki S., Asada M., Tomooka Y., Li A., Yoneda A., Komi A.,
Imamura T.;
"An alternatively-spliced FGF-5 mRNA is abundant in brain and
translates into a partial agonist/antagonist for FGF-5 neurotrophic
activity.";
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
TISSUE=Umbilical artery;
PubMed=10823842; DOI=10.1074/jbc.M910099199;
de Vries C.J.M., van Achterberg T.A.E., Horrevoets A.J.G.,
ten Cate J.W., Pannekoek H.;
"Differential display identification of 40 genes with altered
expression in activated human smooth muscle cells. Local expression in
atherosclerotic lesions of smags, smooth muscle activation-specific
genes.";
J. Biol. Chem. 275:23939-23947(2000).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
PubMed=11454700;
Hanada K.-I., Perry-Lalley D.M., Ohnmacht G.A., Bettinotti M.P.,
Yang J.C.;
"Identification of fibroblast growth factor-5 as an overexpressed
antigen in multiple human adenocarcinomas.";
Cancer Res. 61:5511-5516(2001).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-54.
NIEHS SNPs program;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS SHORT AND LONG).
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
INTERACTION WITH FGFR1 AND FGFR2, AND FUNCTION IN CELL PROLIFERATION.
PubMed=8663044; DOI=10.1074/jbc.271.25.15292;
Ornitz D.M., Xu J., Colvin J.S., McEwen D.G., MacArthur C.A.,
Coulier F., Gao G., Goldfarb M.;
"Receptor specificity of the fibroblast growth factor family.";
J. Biol. Chem. 271:15292-15297(1996).
[11]
REVIEW.
PubMed=20094046; DOI=10.1038/nrc2780;
Turner N., Grose R.;
"Fibroblast growth factor signalling: from development to cancer.";
Nat. Rev. Cancer 10:116-129(2010).
[12]
INVOLVEMENT IN TCMGLY, AND VARIANT TCMGLY HIS-174.
PubMed=24989505; DOI=10.1073/pnas.1402862111;
Higgins C.A., Petukhova L., Harel S., Ho Y.Y., Drill E., Shapiro L.,
Wajid M., Christiano A.M.;
"FGF5 is a crucial regulator of hair length in humans.";
Proc. Natl. Acad. Sci. U.S.A. 111:10648-10653(2014).
-!- FUNCTION: Plays an important role in the regulation of cell
proliferation and cell differentiation. Required for normal
regulation of the hair growth cycle. Functions as an inhibitor of
hair elongation by promoting progression from anagen, the growth
phase of the hair follicle, into catagen the apoptosis-induced
regression phase (By similarity). {ECO:0000250|UniProtKB:Q20FD0,
ECO:0000269|PubMed:8663044}.
-!- SUBUNIT: Interacts with FGFR1 and FGFR2. Affinity between
fibroblast growth factors (FGFs) and their receptors is increased
by heparan sulfate glycosaminoglycans that function as
coreceptors. {ECO:0000269|PubMed:8663044}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=P12034-1; Sequence=Displayed;
Name=Short; Synonyms=FGF-5S;
IsoId=P12034-2; Sequence=VSP_001518, VSP_001519;
Note=Seems to have an antagonistic effect compared to that of
the isoform Long.;
-!- TISSUE SPECIFICITY: Expressed in neonatal brain.
-!- DEVELOPMENTAL STAGE: Can transform NIH 3T3 cells.
-!- DISEASE: Trichomegaly (TCMGLY) [MIM:190330]: A morphologic trait
characterized by unusually long eyelashes and mild hypertrichosis
of eyebrows. It can be observed in association with corneal
irritation, cataracts, and hereditary spherocytosis.
{ECO:0000269|PubMed:24989505}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the heparin-binding growth factors family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB60698.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/fgf5/";
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EMBL; M37825; AAB06463.1; -; mRNA.
EMBL; M23536; AAB60699.1; -; Genomic_DNA.
EMBL; M23534; AAB60699.1; JOINED; Genomic_DNA.
EMBL; M23535; AAB60699.1; JOINED; Genomic_DNA.
EMBL; M23534; AAB60698.1; ALT_SEQ; Genomic_DNA.
EMBL; AB016517; BAA33738.1; -; mRNA.
EMBL; AF171928; AAF89742.1; -; mRNA.
EMBL; AF535149; AAN04097.1; -; mRNA.
EMBL; DQ151636; AAZ67914.1; -; Genomic_DNA.
EMBL; AK291962; BAF84651.1; -; mRNA.
EMBL; AK312065; BAG35001.1; -; mRNA.
EMBL; CH471057; EAX05859.1; -; Genomic_DNA.
EMBL; CH471057; EAX05860.1; -; Genomic_DNA.
EMBL; BC074858; AAH74858.1; -; mRNA.
EMBL; BC074859; AAH74859.1; -; mRNA.
EMBL; BC131502; AAI31503.1; -; mRNA.
CCDS; CCDS34021.1; -. [P12034-1]
CCDS; CCDS3586.1; -. [P12034-2]
PIR; A31194; TVHUF5.
PIR; B31194; B31194.
RefSeq; NP_004455.2; NM_004464.3. [P12034-1]
RefSeq; NP_149134.1; NM_033143.2. [P12034-2]
UniGene; Hs.37055; -.
ProteinModelPortal; P12034; -.
SMR; P12034; -.
BioGrid; 108541; 5.
DIP; DIP-4018N; -.
IntAct; P12034; 4.
STRING; 9606.ENSP00000311697; -.
iPTMnet; P12034; -.
PhosphoSitePlus; P12034; -.
BioMuta; FGF5; -.
DMDM; 85700417; -.
PaxDb; P12034; -.
PeptideAtlas; P12034; -.
PRIDE; P12034; -.
DNASU; 2250; -.
Ensembl; ENST00000312465; ENSP00000311697; ENSG00000138675. [P12034-1]
Ensembl; ENST00000456523; ENSP00000398353; ENSG00000138675. [P12034-2]
GeneID; 2250; -.
KEGG; hsa:2250; -.
UCSC; uc003hmd.4; human. [P12034-1]
CTD; 2250; -.
DisGeNET; 2250; -.
EuPathDB; HostDB:ENSG00000138675.16; -.
GeneCards; FGF5; -.
HGNC; HGNC:3683; FGF5.
HPA; CAB010313; -.
HPA; HPA042442; -.
MalaCards; FGF5; -.
MIM; 165190; gene.
MIM; 190330; phenotype.
neXtProt; NX_P12034; -.
OpenTargets; ENSG00000138675; -.
Orphanet; 411788; Familial isolated trichomegaly.
PharmGKB; PA28122; -.
eggNOG; KOG3885; Eukaryota.
eggNOG; ENOG4111IPH; LUCA.
GeneTree; ENSGT00760000118859; -.
HOGENOM; HOG000236341; -.
HOVERGEN; HBG007580; -.
InParanoid; P12034; -.
KO; K04358; -.
OMA; LSAWAHG; -.
OrthoDB; EOG091G0NAY; -.
PhylomeDB; P12034; -.
TreeFam; TF317805; -.
Reactome; R-HSA-109704; PI3K Cascade.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1839122; Signaling by activated point mutants of FGFR1.
Reactome; R-HSA-1839130; Signaling by activated point mutants of FGFR3.
Reactome; R-HSA-190372; FGFR3c ligand binding and activation.
Reactome; R-HSA-190373; FGFR1c ligand binding and activation.
Reactome; R-HSA-190375; FGFR2c ligand binding and activation.
Reactome; R-HSA-2033514; FGFR3 mutant receptor activation.
Reactome; R-HSA-2033519; Activated point mutants of FGFR2.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-5654219; Phospholipase C-mediated cascade: FGFR1.
Reactome; R-HSA-5654221; Phospholipase C-mediated cascade, FGFR2.
Reactome; R-HSA-5654227; Phospholipase C-mediated cascade, FGFR3.
Reactome; R-HSA-5654687; Downstream signaling of activated FGFR1.
Reactome; R-HSA-5654688; SHC-mediated cascade:FGFR1.
Reactome; R-HSA-5654689; PI-3K cascade:FGFR1.
Reactome; R-HSA-5654693; FRS-mediated FGFR1 signaling.
Reactome; R-HSA-5654695; PI-3K cascade:FGFR2.
Reactome; R-HSA-5654699; SHC-mediated cascade:FGFR2.
Reactome; R-HSA-5654700; FRS-mediated FGFR2 signaling.
Reactome; R-HSA-5654704; SHC-mediated cascade:FGFR3.
Reactome; R-HSA-5654706; FRS-mediated FGFR3 signaling.
Reactome; R-HSA-5654710; PI-3K cascade:FGFR3.
Reactome; R-HSA-5654726; Negative regulation of FGFR1 signaling.
Reactome; R-HSA-5654727; Negative regulation of FGFR2 signaling.
Reactome; R-HSA-5654732; Negative regulation of FGFR3 signaling.
Reactome; R-HSA-5655253; Signaling by FGFR2 in disease.
Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
Reactome; R-HSA-5658623; FGFRL1 modulation of FGFR1 signaling.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-8853338; Signaling by FGFR3 point mutants in cancer.
SIGNOR; P12034; -.
GeneWiki; FGF5; -.
GenomeRNAi; 2250; -.
PRO; PR:P12034; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000138675; -.
CleanEx; HS_FGF5; -.
ExpressionAtlas; P12034; baseline and differential.
Genevisible; P12034; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; TAS:ProtInc.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; TAS:Reactome.
GO; GO:0005104; F:fibroblast growth factor receptor binding; IDA:MGI.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0004713; F:protein tyrosine kinase activity; TAS:Reactome.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IDA:MGI.
GO; GO:0010001; P:glial cell differentiation; IEA:Ensembl.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:MGI.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IEA:Ensembl.
CDD; cd00058; FGF; 1.
InterPro; IPR028240; FGF5.
InterPro; IPR002209; Fibroblast_GF_fam.
InterPro; IPR008996; IL1/FGF.
PANTHER; PTHR11486; PTHR11486; 1.
PANTHER; PTHR11486:SF23; PTHR11486:SF23; 1.
Pfam; PF00167; FGF; 1.
PRINTS; PR00263; HBGFFGF.
SMART; SM00442; FGF; 1.
SUPFAM; SSF50353; SSF50353; 1.
PROSITE; PS00247; HBGF_FGF; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disease mutation;
Glycoprotein; Growth factor; Mitogen; Polymorphism; Proto-oncogene;
Reference proteome; Secreted; Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 268 Fibroblast growth factor 5.
/FTId=PRO_0000008958.
COMPBIAS 49 52 Poly-Ser.
COMPBIAS 55 62 Poly-Ser.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 120 123 VLEI -> QVHR (in isoform Short).
{ECO:0000303|PubMed:10823842,
ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.3}.
/FTId=VSP_001518.
VAR_SEQ 124 268 Missing (in isoform Short).
{ECO:0000303|PubMed:10823842,
ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.3}.
/FTId=VSP_001519.
VARIANT 54 54 M -> V (in dbSNP:rs33950145).
{ECO:0000269|Ref.6}.
/FTId=VAR_025174.
VARIANT 174 174 Y -> H (in TCMGLY; dbSNP:rs587777581).
{ECO:0000269|PubMed:24989505}.
/FTId=VAR_072566.
CONFLICT 42 42 R -> I (in Ref. 1; AAB06463).
{ECO:0000305}.
CONFLICT 83 86 PSGR -> LGA (in Ref. 2; AAB60699).
{ECO:0000305}.
CONFLICT 224 224 Q -> QQ (in Ref. 6; AAZ67914).
{ECO:0000305}.
CONFLICT 238 238 K -> N (in Ref. 1; AAB06463 and 2;
AAB60699). {ECO:0000305}.
CONFLICT 245 245 P -> S (in Ref. 1; AAB06463 and 2;
AAB60699). {ECO:0000305}.
SEQUENCE 268 AA; 29551 MW; 28B7268B26781BCF CRC64;
MSLSFLLLLF FSHLILSAWA HGEKRLAPKG QPGPAATDRN PRGSSSRQSS SSAMSSSSAS
SSPAASLGSQ GSGLEQSSFQ WSPSGRRTGS LYCRVGIGFH LQIYPDGKVN GSHEANMLSV
LEIFAVSQGI VGIRGVFSNK FLAMSKKGKL HASAKFTDDC KFRERFQENS YNTYASAIHR
TEKTGREWYV ALNKRGKAKR GCSPRVKPQH ISTHFLPRFK QSEQPELSFT VTVPEKKKPP
SPIKPKIPLS APRKNTNSVK YRLKFRFG


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E0036h ELISA kit FGF9,FGF-9,Fibroblast growth factor 9,GAF,Glia-activating factor,HBGF-9,Heparin-binding growth factor 9,Homo sapiens,Human 96T


 

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